Peptide chain assembly design

The main goal of this chapter is to describe the synthesis details of complex, orthogonally protected peptide constructs. Thus, major emphasis is placed on the peptide chain assembly design and practice and the alterations from the solid-phase synthesis of simple, nonmodified peptides. The technology for peptide purification and quality control is not significantly different from that of other peptides, and these methods will be just briefly described. Many chapters of this book focus on the optimization of HPLC and MALDI-MS procedures for peptide separation and analysis and illustrate the expected and/or acceptable quality control parameters. 

This chapter focuses on supramolecular assemblies that are formed using a variety of de novo designed peptide-based tectons. A brief introdnction to amino acids (the building blocks of peptides and proteins) is given, followed by a discussion of the basic structures that polypeptide chains of amino acids can adopt. These structures form the basis of the supramolecular assemblies that will be reviewed. The subsequent sections provide details of recent examples of repetitive, effectively infinite, and discrete snpramolecular peptide-based assemblies, and also a dis-cnssion of their potential applications. 

A unique feature of such DNA-directed self-assemblies is their site-selective immobilization, which makes it possible to construct well-defined nanostructures. On the other hand, the possibility of the introduction of a vast number of substitutes (like peptidic sequences, nucleoproteins, of hydrophobic hydrocarbon chains) to an adamantane core (adamantyl) makes such a process capable of designing steric colloidal and supramolecular conformations by setting hydrophobic/hydrophilic and other interactions. In addition, the rigidity of the adamantane structure can provide strength and rigidity to such self-assemblies [150]. 

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